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6 Cards in this Set
- Front
- Back
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Structural Features controlling the protein:DNA binding: |
- most recognition is from the major groove
- match between H bond donation and acceptors
*THE WATSON AND CRICK BASE PAIRING MODEL IS NOT INTERRUPTED FROM THE H BONDING INTERRACTIONS. Although they are base pairing and sharing with DNA, they are doing nothing to disrupt the base pairing; so DNA stays ds, and they can make interactions with AA side chains.
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Structural Features of DNA Binding Domains: |
- helix-turn-helix - zinc finger is the MOST COMMON motif in regulatory factors. It fits into the major groove. - basic region - beta sheet - winged-helix |
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Structural Features of Activation Domains: |
- acidic domain - glutamine rich domain - proline rich domain - ser/thr rich domain |
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Enhancesome: |
multiple reg factors assemble on a gene promoter to control gene expression.
held in place by DNA:protein interaction and protein: protein interaction with HMG1 (which binds to the minor groove) that helps stabilize that interaction. |
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Why is TBP found in all polymerases and even in CpG islands? |
Because it is held in place by protein:protein interactions (in the minor groove), not by AAs and H bonding interactions like the TATA box. |
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Mediator Complex: |
Molecular bridge between activators and pol II (during trans-activation domains of regulatory factors and pol II).
Has alpha helical coils that help to form a scaffold.
They promote the assembly of the complex and the phosphorylation of pol II; it helps with looping the promoter to help facilitate interaction between reg factors and pol II. |
